6D1X
N-Domain Of Grp94, with the Charged Domain, In Complex With the Novel Ligand N-Propyl Carboxyamido Adenosine
Replaces: 1U0YFunctional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue PA7 A 401 |
Chain | Residue |
A | ASN107 |
A | HOH519 |
A | HOH527 |
A | HOH533 |
A | HOH549 |
A | ALA111 |
A | ASP149 |
A | MET154 |
A | ASN162 |
A | LEU163 |
A | VAL197 |
A | PHE199 |
A | TYR200 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue PG4 A 402 |
Chain | Residue |
A | LEU117 |
A | THR121 |
A | THR212 |
A | ARG237 |
A | THR240 |
A | PG4403 |
A | HOH573 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue PG4 A 403 |
Chain | Residue |
A | LYS137 |
A | TRP282 |
A | PG4402 |
A | HOH562 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue PG4 A 404 |
Chain | Residue |
A | ASN83 |
A | LYS87 |
A | LYS87 |
A | ILE90 |
A | SER227 |
A | HOH564 |
A | HOH574 |
Functional Information from PROSITE/UniProt
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE |
Chain | Residue | Details |
A | TYR94-GLU103 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V |
Chain | Residue | Details |
A | ASN107 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V |
Chain | Residue | Details |
A | ASP149 | |
A | PHE199 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V |
Chain | Residue | Details |
A | ASN162 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625 |
Chain | Residue | Details |
A | LYS168 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0 |
Chain | Residue | Details |
A | SER172 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CK2 => ECO:0000255 |
Chain | Residue | Details |
A | THR288 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255 |
Chain | Residue | Details |
A | SER306 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN107 | |
A | ASN217 |